Animal Bioscience

Asian Australasian Association of Animal Production Societies (아세아태평양축산학회)
권호 표지
DOI QR코드

DOI QR Code

Effect of myoglobin, hemin, and ferric iron on quality of chicken breast meat

  • Zhang, Muhan (Institute of Agricultural Products Processing, Jiangsu Academy of Agricultural Sciences) ;
  • Yan, Weili (Institute of Agricultural Products Processing, Jiangsu Academy of Agricultural Sciences) ;
  • Wang, Daoying (Institute of Agricultural Products Processing, Jiangsu Academy of Agricultural Sciences) ;
  • Xu, Weimin (Institute of Agricultural Products Processing, Jiangsu Academy of Agricultural Sciences)
  • Received : 2020.07.27
  • Accepted : 2020.11.08
  • Published : 2021.08.01
Download PDF
⟨ Previous Next ⟩

Abstract

Objective: The objective was to evaluate the impact of different forms of iron including myoglobin, hemin, and ferric chloride on the quality of chicken breast meat. Methods: Chicken breast muscles were subjected to 1, 2, 3 mg/mL of FeCl3, myoglobin and hemin treatment respectively, and the production of reactive oxygen species (ROS) and malondialdehyde, meat color, tenderness, water holding capacity and morphology of meat was evaluated. Results: Hemin was found to produce more ROS and induce greater extent of lipid oxidation than myoglobin and ferric chloride. However, it showed that hemin could significantly increase the redness and decrease the lightness of the muscle. Hemin was also shown to be prominent in improving water holding capacity of meat, maintaining a relatively higher level of the immobilized water from low-field nuclear magnetic resonance measurements. Morphology observation by hematoxylin-eosin staining further confirmed the results that hemin preserved the integrity of the muscle. Conclusion: The results indicated that hemin may have economic benefit for the industry based on its advantage in improving water holding capacity and quality of meat.

Keywords

Acknowledgement

This study was supported by National Natural Science Foundation of China (31972137), China Agriculture Research System (CARS-41), Primary Research & Development Plan of Jiangsu Province (BE2017392), the Priority Academic Program Development of Jiangsu Higher Education Institutions, Overseas Expertise Introduction Center for Discipline Innovation (111 Center) On Quality & Safety Control and Nutrition of Muscle Food (B14023).

References

  1. Ordway GA, Garry DJ. Myoglobin: an essential hemoprotein in striated muscle. J Exp Biol 2004;207:3441-6. https://doi.org/10.1242/jeb.01172
  2. Giaretta N, Giuseppe AMAD, Lippert M, Parente A, Maro AD. Myoglobin as marker in meat adulteration: a UPLC method for determining the presence of pork meat in raw beef burger. Food Chem 2013;141:1814-20. https://doi.org/10.1016/j.foodchem.2013.04.124
  3. Suman SP, Joseph P. Myoglobin chemistry and meat color. Annu Rev Food Sci Technol 2013;4:79-99. https://doi.org/10.1146/annurev-food-030212-182623
  4. Carlsen CU, Moller JKS, Skibsted LH. Heme-iron in lipid oxidation. Coord Chem Rev 2005;249:485-98. https://doi.org/10.1016/j.ccr.2004.08.028
  5. Maitra D, Byun J, Andreana PR, et al. Reaction of hemoglobin with HOCl: mechanism of heme destruction and free iron release. Free Radic Biol Med 2011;51:374-86. https://doi.org/10.1016/j.freeradbiomed.2011.04.011
  6. Min B, Cordray JC, Ahn DU. Effect of NaCl, myoglobin, Fe (II), and Fe (III) on lipid oxidation of raw and cooked chicken breast and beef loin. J Agric Food Chem 2010;58:600-5. https://doi.org/10.1021/jf9029404
  7. Grunwald EW, Richards MP. Studies with myoglobin variants indicate that released hemin is the primary promoter of lipid oxidation in washed fish muscle. J Agric Food Chem 2006; 54:4452-60. https://doi.org/10.1021/jf0603228
  8. Mokrani A, Krisa S, Cluzet S, et al. Phenolic contents and bioactive potential of peach fruit extracts. Food Chem 2016; 202:212-20. https://doi.org/10.1016/j.foodchem.2015.12.026
  9. Sorensen G, Jorgensen SS. A critical examination of some experimental variables in the 2-thiobarbituric acid (TBA) test for lipid oxidation in meat products. Z Lebensm Unters Forsch 1996;202:205-10. https://doi.org/10.1007/BF01263541
  10. Meullenet JF, Jonville E, Grezes D, Owens CM. Prediction of the texture of cooked poultry pectoralis major muscles by near-infrared reflectance analysis of raw meat. J Texture Stud 2004;35:573-85. https://doi.org/10.1111/j.1538-7836.2004.01165.x-i1
  11. Bertram HC, Oksbjerg N, Young JF. NMR-based metabonomics reveals relationship between pre-slaughter exercise stress, the plasma metabolite profile at time of slaughter, and waterholding capacity in pigs. Meat Sci 2010;84:108-13. https://doi.org/10.1016/j.meatsci.2009.08.031
  12. Lan X, Zhang X, Zhou G, Wu C, Li C, Xu X. Electro-acupuncture reduces apoptotic index and inhibits p38 mitogen-activated protein kinase signaling pathway in the hippocampus of rats with cerebral ischemia/reperfusion injury. Neural Regen Res 2017;12:409-16. https://doi.org/10.4103/1673-5374.202944
  13. Gueraud F, Atalay M, Bresgen N, et al. Chemistry and biochemistry of lipid peroxidation products. Free Radic Res 2010; 44:1098-124. https://doi.org/10.3109/10715762.2010.498477
  14. Yu Y, Mukherjee A, Nilges MJ, Hosseinzadeh P, Miner KD, Lu Y. Direct EPR observation of a tyrosyl radical in a functional oxidase model in myoglobin during both H2O2 and O2 reactions. J Am Chem Soc 2014;136:1174-7. https://doi.org/10.1021/ja4091885
  15. Rhee KS, Ziprin YA. Lipid oxidation in retail beef, pork and chicken muscles as affected by concentrations of heme pigments and nonheme iron and microsomal enzymic lipid peroxidation activity. J Food Biochem 1987;11:1-15. https://doi.org/10.1111/j.1745-4514.1987.tb00109.x
  16. Roginsky V, Zheltukhina GA, Nebolsin VE. Efficacy of metmyoglobin and hemin as a catalyst of lipid peroxidation determined by using a new testing system. J Agric Food Chem 2007;55:6798-806. https://doi.org/10.1021/jf0714362
  17. Vernier G, Chenal A, Vitrac H, Barumandzadhe R, Montagner C, Forge V. Interactions of apomyoglobin with membranes: mechanisms and effects on heme uptake. Protein Sci 2007;16: 391-400. https://doi.org/10.1110/ps.062531207
  18. Baron CP, Andersen HJ. Myoglobin-induced lipid oxidation. A review. J Agric Food Chem 2002;50:3887-97. https://doi.org/10.1021/jf011394w
  19. Mozuraityte R, Rustad T, Storro I. The role of iron in peroxidation of polyunsaturated fatty acids in liposomes. J Agric Food Chem 2008;56:537-43. https://doi.org/10.1021/jf0716073
  20. Cheng Z, Li Y. What is responsible for the initiating chemistry of iron-mediated lipid peroxidation: an update. Chem Rev 2007;107:748-66. https://doi.org/10.1021/cr040077w
  21. Giri RP, Mukhopadhyay MK, Basak UK, et al. Continuous uptake or saturation- investigation of concentration and surface-packing-specific hemin interaction with lipid membranes. J Phys Chem B 2018;122:7547-54. https://doi.org/10.1021/acs.jpcb.8b03327
  22. Faustman C, Sun Q, Mancini R, Suman SP. Myoglobin and lipid oxidation interactions: mechanistic bases and control. Meat Sci 2010;86:86-94. https://doi.org/10.1016/j.meatsci.2010.04.025
  23. Zhou C, Tan S, Li J, Chu X, Cai K. A novel method to stabilize meat colour: ligand coordinating with hemin. J Food Sci Technol 2014;51:1213-7. https://doi.org/10.1007/s13197-012-0625-z
  24. Zhang W, Xiao S, Ahn DU. Protein oxidation: basic principles and implications for meat quality. Crit Rev Food Sci Nutr 2013;53:1191-201. https://doi.org/10.1080/10408398.2011.577540
  25. Lund MN, Luxford C, Skibsted LH, Davies MJ. Oxidation of myosin by haem proteins generates myosin radicals and protein cross-links. Biochem J 2008;410:565-74. https://doi.org/10.1042/BJ20071107
  26. Malheiros JM, Braga CP, Grove RA, et al. Influence of oxidative damage to proteins on meat tenderness using a proteomics approach. Meat Sci 2019;148:64-71. https://doi.org/10.1016/j.meatsci.2018.08.016
  27. Shao JH, Deng YM, Jia N, et al. Low-field NMR determination of water distribution in meat batters with NaCl and polyphosphate addition. Food Chem 2016;200:308-14. https://doi.org/10.1016/j.foodchem.2016.01.013
  28. Huff-Lonergan E, Lonergan SM. Mechanisms of water-holding capacity of meat: the role of postmortem biochemical and structural changes. Meat Sci 2005;71:194-204. https://doi.org/10.1016/j.meatsci.2005.04.022
  29. Barbut S, Zhang L, Marcone M. Effects of pale, normal, and dark chicken breast meat on microstructure, extractable proteins, and cooking of marinated fillets. Poult Sci 2005; 84:797-802. https://doi.org/10.1093/ps/84.5.797
  30. Zhang WG, Lonergan SM, Gardner MA, Huff-Lonergan E. Contribution of postmortem changes of integrin, desmin and μ-calpain to variation in water holding capacity of pork. Meat Sci 2006;74:578-85. https://doi.org/10.1016/j.meatsci.2006.05.008
  31. Wang Z, He Z, Emara AM, Gan X, Li H. Effects of malondialdehyde as a byproduct of lipid oxidation on protein oxidation in rabbit meat. Food Chem 2019;288:405-12. https://doi.org/10.1016/j.foodchem.2019.02.126
  32. Lai JF, Dobbs J, Dunn MA. Evaluation of clams as a food source of iron: total iron, heme iron, aluminum, and in vitro iron bioavailability in live and processed clams. J Food Compost Anal 2012;25:47-55. https://doi.org/10.1016/j.jfca.2011.07.004